[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis; DOI=10.1016/0022-2836(87)90323-8; PubMed=2821268 [NCBI, ExPASy, EBI, Israel, Japan] Davidson E., Daldal F.; "Primary structure of the bc1 complex of Rhodopseudomonas capsulata. Nucleotide sequence of the pet operon encoding the Rieske cytochrome b, and cytochrome c1 apoproteins."; J. Mol. Biol. 195:13-24(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=GA; PubMed=3004982 [NCBI, ExPASy, EBI, Israel, Japan] Gabellini N., Sebald W.; "Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c1."; Eur. J. Biochem. 154:569-579(1986).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95, AND SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:3004982 ORIGINATES FROM RHODOBACTER CAPSULATUS. DOI=10.1016/0022-2836(87)90324-X; PubMed=2821272 [NCBI, ExPASy, EBI, Israel, Japan] Davidson E., Daldal F.; "fbc operon, encoding the Rieske Fe-S protein cytochrome b, and cytochrome c1 apoproteins previously described from Rhodopseudomonas sphaeroides, is from Rhodopseudomonas capsulata."; J. Mol. Biol. 195:25-29(1987).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23. STRAIN=MT1131; PubMed=1323023 [NCBI, ExPASy, EBI, Israel, Japan] Tokito M.K., Daldal F.; "petR, located upstream of the fbcFBC operon encoding the cytochrome bc1 complex, is homologous to bacterial response regulators and necessary for photosynthetic and respiratory growth of Rhodobacter capsulatus."; Mol. Microbiol. 6:1645-1654(1992).
[5]	MUTAGENESIS. STRAIN=MT0-404; DOI=10.1021/bi00128a006; PubMed=1313292 [NCBI, ExPASy, EBI, Israel, Japan] Davidson E., Ohnishi T., Atta-Asafo-Adjei E., Daldal F.; "Potential ligands to the [2Fe-2S] Rieske cluster of the cytochrome bc1 complex of Rhodobacter capsulatus probed by site-directed mutagenesis."; Biochemistry 31:3342-3351(1992).

Comments

FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
CATALYTIC ACTIVITY: QH₂ + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H⁺.
COFACTOR: Binds 1 2Fe-2S cluster per subunit.
SUBUNIT: The main subunits of complex b-c1 are: cytochrome b, cytochrome c1 and the Rieske protein.
SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
SIMILARITY: Contains 1 Rieske domain.
CAUTION: The sequence reported in PubMed:3004982 was thought to originate from R.sphaeroides but was later shown (PubMed:2821272) to be derived from R.capsulatus.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X05630; CAA29116.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18576; AAA26151.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z12113; CAA78099.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03476; CAA27194.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29336; A29336.

3D structure databases

PDB

1ZRT; X-ray; 3.50 A; E/R=1-191.

[ExPASy / RCSB / EBI]

PDBsum

1ZRT; -.

ModBase

P08500.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008121;	Molecular function: ubiquinol-cytochrome-c reductase activity (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR014349; Rieske.
IPR005805; Rieske_C.
IPR006317; Rieske_proteo.
IPR005806; Rieske_reg.
IPR006311; Tat.
Graphical view of domain structure.

Gene3D

G3DSA:2.102.10.10; Rieske_reg; 1.

PANTHER

PTHR10134; Rieske; 1.

Pfam

PF00355; Rieske; 1.
Pfam graphical view of domain structure.

PRINTS

PR00162; RIESKE.

TIGRFAMs

TIGR01416; Rieske_proteo; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

PS51296; RIESKE; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

P08500.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; 3D-structure; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 191`	`191`	`Ubiquinol-cytochrome c reductase iron-sulfur subunit.`	`PRO_0000127762`
`TRANSMEM`	`18 35`	`18`	`Potential.`
`DOMAIN`	`94 189`	`96`	`Rieske.`
`METAL`	`133 133`		`Iron-sulfur (2Fe-2S).`
`METAL`	`135 135`		`Iron-sulfur (2Fe-2S); via pros nitrogen.`
`METAL`	`153 153`		`Iron-sulfur (2Fe-2S).`
`METAL`	`156 156`		`Iron-sulfur (2Fe-2S); via pros nitrogen.`
`DISULFID`	`138 155`
`VARIANT`	`48 48`	`1`	`A -> S (in strain: GA).`
`VARIANT`	`114 114`	`1`	`T -> S (in strain: GA).`
`VARIANT`	`116 116`	`1`	`P -> A (in strain: GA).`
`MUTAGEN`	`133 133`		`C->R,S: Photosynthetically incompetent.`
`MUTAGEN`	`135 135`		`H->L,P: Photosynthetically incompetent.`
`MUTAGEN`	`138 138`		`C->F,R,S: Photosynthetically incompetent.`
`MUTAGEN`	`153 153`		`C->R,S: Photosynthetically incompetent.`
`MUTAGEN`	`155 155`		`C->D,G,S: Photosynthetically incompetent.`
`MUTAGEN`	`156 156`		`H->L,P,F: Photosynthetically incompetent.`
`MUTAGEN`	`156 156`		`H->T,Y: Photosynthetically incompetent.`
`MUTAGEN`	`159 159`		`H->A,S: Photosynthetically competent.`
`HELIX`	`12 37`	`26`
`HELIX`	`43 45`	`3`
`STRAND`	`50 52`	`3`
`STRAND`	`63 67`	`5`
`STRAND`	`70 75`	`6`
`HELIX`	`79 86`	`8`
`STRAND`	`90 92`	`3`
`STRAND`	`101 103`	`3`
`HELIX`	`110 114`	`5`
`STRAND`	`119 121`	`3`
`STRAND`	`127 129`	`3`
`STRAND`	`134 136`	`3`
`STRAND`	`146 148`	`3`
`TURN`	`154 156`	`3`
`STRAND`	`166 170`	`5`
`STRAND`	`179 186`	`8`
`STRAND`	`188 190`	`3`

Sequence information

Length: 191 AA [This is the length of the unprocessed precursor]

Molecular weight: 20440 Da [This is the MW of the unprocessed precursor]

CRC64: E7D496405154D5F4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSHAEDNAGT RRDFLYHATA ATGVVVTGAA VWPLINQMNA SADVKAMASI FVDVSAVEVG 

        70         80         90        100        110        120 
TQLTVKWRGK PVFIRRRDEK DIELARSVPL GALRDTSAEN ANKPGAEATD ENRTLPAFDG 

       130        140        150        160        170        180 
TNTGEWLVML GVCTHLGCVP MGDKSGDFGG WFCPCHGSHY DSAGRIRKGP APRNLDIPVA 

       190 
AFVDETTIKL G

P08500 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools